메뉴 건너뛰기




Volumn 51, Issue 1, 2012, Pages 83-89

Head-to-tail interaction between amphotericin b and ergosterol occurs in hydrated phospholipid membrane

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOTERICIN B; ANTI-FUNGAL ACTIVITY; BI-LAYER; BILAYER SURFACE; DEPHASING; ION CHANNEL; PHOSPHOLIPID BILAYER; PHOSPHOLIPID MEMBRANE; PHOSPHORUS ATOM; REDOR EXPERIMENTS; ROTATIONAL ECHO DOUBLE RESONANCE; SIDE-CHAINS;

EID: 84856839893     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2012542     Document Type: Article
Times cited : (35)

References (50)
  • 1
    • 0030449320 scopus 로고    scopus 로고
    • Amphotericin B: New life for an old drug
    • DOI 10.1016/S0165-6147(96)01012-7
    • Hartsel, S., and Bolard, J. (1996) Amphotericin B: new life for an old drug. Trends Pharmacol. Sci. 17, 445-449. (Pubitemid 27028476)
    • (1996) Trends in Pharmacological Sciences , vol.17 , Issue.12 , pp. 445-449
    • Hartsel, S.1    Bolard, J.2
  • 3
    • 0015980909 scopus 로고
    • Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes 3. Molecular structure of the polyene antibioticcholesterol complexes
    • De Kruijff, B., and Demel, R. A. (1974) Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes. 3. Molecular structure of the polyene antibioticcholesterol complexes. Biochim. Biophys. Acta 339, 57-70.
    • (1974) Biochim. Biophys. Acta , vol.339 , pp. 57-70
    • De Kruijff, B.1    Demel, R.A.2
  • 4
    • 0025808089 scopus 로고
    • Onesided action of amphotericin B on cholesterol-containing membranes is determined by its self-association in the medium
    • Bolard, J., Legrand, P., Heitz, F., and Cybulska, B. (1991) Onesided action of amphotericin B on cholesterol-containing membranes is determined by its self-association in the medium. Biochemistry 30, 5707-5715.
    • (1991) Biochemistry , vol.30 , pp. 5707-5715
    • Bolard, J.1    Legrand, P.2    Heitz, F.3    Cybulska, B.4
  • 5
    • 0020068655 scopus 로고
    • Equilibrium binding of amphotericin B and its methyl ester and borate complex to sterols
    • Readio, J. D., and Bittman, R. (1982) Equilibrium binding of amphotericin B and its methyl ester and borate complex to sterols. Biochim. Biophys. Acta 685, 219-224. (Pubitemid 12153839)
    • (1982) Biochimica et Biophysica Acta , vol.685 , Issue.2 , pp. 219-224
    • Readio, J.D.1    Bittman, R.2
  • 6
    • 0021992852 scopus 로고
    • Rates of amphotericin B and filipin association with sterols
    • Clejan, S., and Bittoman, R. (1985) Rates of amphotericin B and filipin association with sterols. J. Biol. Chem. 260, 2884-2889.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2884-2889
    • Clejan, S.1    Bittoman, R.2
  • 7
    • 0030933186 scopus 로고    scopus 로고
    • The formation of amphotericin B ion channels in lipid bilayers
    • DOI 10.1021/bi962894z
    • Fujii, G., Chang, J. E., Coley, T., and Steere, B. (1997) The formation of amphotericin B ion channel in lipid bilayers. Biochemistry 36, 4959-4968. (Pubitemid 27180978)
    • (1997) Biochemistry , vol.36 , Issue.16 , pp. 4959-4968
    • Fujii, G.1    Chang, J.-E.2    Coley, T.3    Steere, B.4
  • 8
    • 23044484361 scopus 로고    scopus 로고
    • Mycosamine orientation of amphotericin B controlling interaction with ergosterol: Sterol-dependent activity of conformation-restricted derivatives with an amino-carbonyl bridge
    • DOI 10.1021/ja051597r
    • Matsumori, N., Sawada, Y., and Murata, M. (2005) Mycosamine orientation of amphotericin B controlling interaction with ergosterol: Sterol-dependent activity of conformation-restricted derivatives with amino-carbonyl bridge. J. Am. Chem. Soc. 127, 10667-10675. (Pubitemid 41061440)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.30 , pp. 10667-10675
    • Matsumori, N.1    Sawada, Y.2    Murata, M.3
  • 9
    • 79952590274 scopus 로고    scopus 로고
    • Probing the role of the mycosamine C2'-OH on the activity of amphotericin B
    • Croatt, M. P., and Carreira, E. M. (2011) Probing the role of the mycosamine C2'-OH on the activity of amphotericin B. Org. Lett. 13, 1390-1393.
    • (2011) Org. Lett. , vol.13 , pp. 1390-1393
    • Croatt, M.P.1    Carreira, E.M.2
  • 10
    • 46749087921 scopus 로고    scopus 로고
    • Synthesis and biological studies of 35-deoxy amphotericin B methyl ester
    • Szpilman, A. M., Manthorpe, J. M., and Carreira, E. M. (2008) Synthesis and biological studies of 35-deoxy amphotericin B methyl ester. Angew. Chem., Int. Ed. 47, 4339-4342.
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 4339-4342
    • Szpilman, A.M.1    Manthorpe, J.M.2    Carreira, E.M.3
  • 11
    • 36148980794 scopus 로고    scopus 로고
    • A post-PKS oxidation of the amphotericin B skeleton predicted to be critical for channel formation is not required for potent antifungal activity
    • DOI 10.1021/ja075739o
    • Palacios, D. S., Anderson, T. M., and Burke, M. D. (2007) A post-PKS oxidation of the amphotericin B skeleton predicted to be critical for channel formation is not required for potent antifungal activity. J. Am. Chem. Soc. 129, 13804-13805. (Pubitemid 350106059)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.45 , pp. 13804-13805
    • Palacios, D.S.1    Anderson, T.M.2    Burke, M.D.3
  • 12
    • 79955563191 scopus 로고    scopus 로고
    • Synthesis-enabled functional group deletions reveal key underpinnings of amphotericin B ion channel and antifungal activities
    • Palacios, D. S., Dailey, I., Siebert, D. M., Wilcock, B. C., and Burke, M. D. (2011) Synthesis-enabled functional group deletions reveal key underpinnings of amphotericin B ion channel and antifungal activities. Proc. Natl. Acad. Sci. U. S. A. 108, 6733-6738.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6733-6738
    • Palacios, D.S.1    Dailey, I.2    Siebert, D.M.3    Wilcock, B.C.4    Burke, M.D.5
  • 13
    • 0036467322 scopus 로고    scopus 로고
    • Interactions of the drug amphotericin B with phospholipid membranes containing or not ergosterol: New insight into the role of ergosterol
    • DOI 10.1016/S0005-2736(01)00416-3, PII S0005273601004163
    • Milhaud, J., Ponsinet, V., Takashi, M., and Michels, B. (2002) Interactions of the drug amphotericin B with phospholipid membranes containing or not ergosterol: new insight into the role of ergosterol. Biochim. Biophys. Acta 1558, 95-108. (Pubitemid 34075525)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1558 , Issue.2 , pp. 95-108
    • Milhaud, J.1    Ponsinet, V.2    Takashi, M.3    Michels, B.4
  • 14
    • 18544401585 scopus 로고    scopus 로고
    • The effect of aggregation state of amphotericin-B on its interactions with cholesterol- or ergo sterol-containing phosphatidylcholine monolayers
    • DOI 10.1016/S0009-3084(96)02652-7, PII S0009308496026527
    • Barwicz, J., and Tancrède, P. (1997) The effect of aggregation state of amphotericin-B on its interactions with cholesterol-or ergosterol-containing phosphatidylcholine monolayers. Chem. Phys. Lipids 85, 145-155. (Pubitemid 27129792)
    • (1997) Chemistry and Physics of Lipids , vol.85 , Issue.2 , pp. 145-155
    • Barwicz, J.1    Tancrede, P.2
  • 15
    • 48249090423 scopus 로고    scopus 로고
    • Complex formation of amphotericin B in sterol-containing membrane as evidenced by surface plasmon resonance
    • Mouri, R., Konoki, K., Matsumori, N., Oishi, T., and Murata, M. (2008) Complex formation of amphotericin B in sterol-containing membrane as evidenced by surface plasmon resonance. Biochemistry 47, 7807-7815.
    • (2008) Biochemistry , vol.47 , pp. 7807-7815
    • Mouri, R.1    Konoki, K.2    Matsumori, N.3    Oishi, T.4    Murata, M.5
  • 17
    • 0020637999 scopus 로고
    • Differences in the interaction of the polyene antibiotic amphotericin B with cholesterol- or ergosterol-containing phospholipid vesicles. A circular dichroism and permeability study
    • Vertut-Croquin, A., Bolard, J., Chabbert, M., and Gary-Bobo, C. (1983) Differences in the interaction of the polyene antibiotic amphotericin B with cholesterol-or ergosterol-containing phospholipid vesicles. A circular dichroism and permeability study. Biochemistry 22, 2939-2944. (Pubitemid 13042790)
    • (1983) Biochemistry , vol.22 , Issue.12 , pp. 2939-2944
    • Vertut Croquin, A.1    Bolard, J.2    Chabbert, M.3    Gary Bobo, C.4
  • 18
    • 0026777510 scopus 로고
    • A sequential mechanism for the formation of aqueous channels by amphotericin B in liposomes the effect of sterols and phospholipid composition
    • Cohen, B. E. (1992) A sequential mechanism for the formation of aqueous channels by amphotericin B in liposomes. The effect of sterols and phospholipid composition. Biochim. Biophys. Acta 1108, 49-58.
    • (1992) Biochim. Biophys. Acta , vol.1108 , pp. 49-58
    • Cohen, B.E.1
  • 19
    • 69549112861 scopus 로고    scopus 로고
    • Formation of two different types of ion channels by amphotericin B in human erythrocyte membranes
    • Romero, E. A., Valdivieso, E., and Cohen, B. E. (2009) Formation of two different types of ion channels by amphotericin B in human erythrocyte membranes. J. Membr. Biol. 230, 69-81.
    • (2009) J. Membr. Biol. , vol.230 , pp. 69-81
    • Romero, E.A.1    Valdivieso, E.2    Cohen, B.E.3
  • 20
    • 78650608765 scopus 로고    scopus 로고
    • How do sterols determine the antifungal activity of amphotericin B? Free energy of binding between the drug and its membrane targets
    • Neumann, A., Baginski, M., and Czub, J. (2010) How do sterols determine the antifungal activity of amphotericin B? Free energy of binding between the drug and its membrane targets. J. Am. Chem. Soc. 132, 18266-18272.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 18266-18272
    • Neumann, A.1    Baginski, M.2    Czub, J.3
  • 21
    • 0021151263 scopus 로고
    • Interaction of amphotericin B with membrane lipids as viewed by 2H NMR
    • Dufourc, E. J., Smith, J. C. P., and Jarrell, H. C. (1984) Interaction of amphotericin B with membrane lipids as viewed by 2H NMR. Biochim. Biophys. Acta 776, 317-329.
    • (1984) Biochim. Biophys. Acta , vol.776 , pp. 317-329
    • Dufourc, E.J.1    Smith, J.C.P.2    Jarrell, H.C.3
  • 22
    • 69049089792 scopus 로고    scopus 로고
    • Direct interaction between amphotericin B and ergosterol in lipid bilayers as revealed by 2H NMR spectroscopy
    • Matsumori, N., Tahara, K., Yamamoto, H., Morooka, A., Doi., M., Oishi, T., and Murata, M. (2009) Direct interaction between amphotericin B and ergosterol in lipid bilayers as revealed by 2H NMR spectroscopy. J. Am. Chem. Soc. 131, 11855-11860.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 11855-11860
    • Matsumori, N.1    Tahara, K.2    Yamamoto, H.3    Morooka, A.4    Doi, M.5    Oishi, T.6    Murata, M.7
  • 23
    • 0344291484 scopus 로고    scopus 로고
    • Comparative molecular dynamics simulations of amphotericin B-cholesterol/ergosterol membrane channels
    • DOI 10.1016/S0005-2736(02)00581-3, PII S0005273602005813
    • Baginski, M., Resat, H., and Borowski, E. (2002) Comparative molecular dynamics simulations of amphotericin B-cholesterol/ ergosterol membrane channels. Biochim. Biophys. Acta 1567, 63-78. (Pubitemid 35454048)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1567 , Issue.SUPPL. , pp. 63-78
    • Baginski, M.1    Resat, H.2    Borowski, E.3
  • 24
    • 0032516750 scopus 로고    scopus 로고
    • The structuring effects of amphotericin B on pure and ergosterol- or cholesterol-containing dipalmitoylphosphatidylcholine bilayers: A differential scanning calorimetry study
    • DOI 10.1016/S0005-2736(98)00083-2, PII S0005273698000832
    • Fournier, I., Barwicz, J., and Tancrède, P. (1998) The structuring effects of amphotericin B on pure and ergosterol-or cholesterolcontaining dipalmitoylphosphatidylcholine bilayers: a differential scanning calorimetry study. Biochim. Biophys. Acta 1373, 76-86. (Pubitemid 28495668)
    • (1998) Biochimica et Biophysica Acta - Biomembranes , vol.1373 , Issue.1 , pp. 76-86
    • Fournier, I.1    Barwicz, J.2    Tancrede, P.3
  • 25
    • 0036774484 scopus 로고    scopus 로고
    • 2H NMR
    • DOI 10.1016/S0009-3084(02)00071-3, PII S0009308402000713
    • Paquet, M. J., Fournier, I., Barwicz, J., Tancrède, P., and Auger, M. (2002) The effects of amphotericin B on pure and ergosterol-or cholesterol-containing dipalmitoylphosphatidylcholine bilayers as viewed by 2H NMR. Chem. Phys. Lipids 119, 1-11. (Pubitemid 35247912)
    • (2002) Chemistry and Physics of Lipids , vol.119 , Issue.1-2 , pp. 1-11
    • Paquet, M.-J.1    Fournier, I.2    Barwicz, J.3    Tancrede, P.4    Auger, M.5
  • 26
    • 38849205715 scopus 로고    scopus 로고
    • Self-assembled amphotericin B is probably surrounded by ergosterol: Bimolecular interactions as evidenced by solid-state NMR and CD spectra
    • DOI 10.1002/chem.200701256
    • Kasai, Y., Matsumori, N., Umegawa, Y., Matsuoka, S., Ueno, H., Ikeuchi, H., Oishi, T., and Murata, M. (2008) Self-assembled amphotericin B is probably surrounded by ergosterol: Bimolecular interactions as evidenced by solid-state NMR and CD spectra. Chem.?Eur. J. 14, 1178-1185. (Pubitemid 351204601)
    • (2008) Chemistry - A European Journal , vol.14 , Issue.4 , pp. 1178-1185
    • Kasai, Y.1    Matsumori, N.2    Umegawa, Y.3    Matsuoka, S.4    Ueno, H.5    Ikeuchi, H.6    Oishi, T.7    Murata, M.8
  • 27
    • 58149165036 scopus 로고    scopus 로고
    • Ergosterol increases intermolecular distance of amphotericin B in membrane-bound assembly as evidenced by solid-state NMR
    • Umegawa, Y., Matsumori, N., Oishi, T., and Murata, M. (2008) Ergosterol increases intermolecular distance of amphotericin B in membrane-bound assembly as evidenced by solid-state NMR. Biochemistry 47, 13463-13469.
    • (2008) Biochemistry , vol.47 , pp. 13463-13469
    • Umegawa, Y.1    Matsumori, N.2    Oishi, T.3    Murata, M.4
  • 28
    • 0345448252 scopus 로고    scopus 로고
    • Membrane permeabilizing activity of amphotericin B is affected by chain length of phosphatidylcholine added as minor constituent
    • DOI 10.1016/j.bbamem.2003.09.010
    • Matsuoka, S., and Murata, M. (2003) Membrane permeabilizing activity of amphotericin B is affected by chain length of phosphatidylcholine added as minor constituent. Biochim. Biophys. Acta 1617, 109-115. (Pubitemid 37456718)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1617 , Issue.1-2 , pp. 109-115
    • Matsuoka, S.1    Murata, M.2
  • 29
    • 12144279187 scopus 로고    scopus 로고
    • 31P rotational echo double resonance
    • DOI 10.1021/bi049001k
    • Matsuoka, S., Ikeuchi, H., Matsumori, N., and Murata, M. (2005) Dominant formation of a single-length channel by amphotericin B in dimyristoylphosphatidylcholine membrane evidenced by 13C-31P rotational echo double resonance. Biochemistry 44, 704-710. (Pubitemid 40105501)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 704-710
    • Matsuoka, S.1    Ikeuchi, H.2    Matsumori, N.3    Murata, M.4
  • 32
    • 0011392614 scopus 로고
    • Biosynthesis of sitosterol, cycloartenol, and 24-methylenecycloartanol in tissue cultures of higher plants and of ergosterol in yeast from [1,2-13C2]-and [2-13C2H3]-acetate and [5-13C2H2]MVA
    • Seo, S., Uomori, A., Yoshimura, Y., Takeda, K., Seto, H., Ebizuka, Y., Noguchi, H., and Sankawa, U. (1988) Biosynthesis of sitosterol, cycloartenol, and 24-methylenecycloartanol in tissue cultures of higher plants and of ergosterol in yeast from [1,2-13C2]-and [2-13C2H3]-acetate and [5-13C2H2]MVA. J. Chem. Soc., Perkin Trans. 1, 2407-2414.
    • (1988) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 2407-2414
    • Seo, S.1    Uomori, A.2    Yoshimura, Y.3    Takeda, K.4    Seto, H.5    Ebizuka, Y.6    Noguchi, H.7    Sankawa, U.8
  • 33
    • 46649110735 scopus 로고    scopus 로고
    • Influence of temperature on 31P NMR chemical shifts of phospholipids and their metabolites i in chloroform-methanol-water
    • Estrada, R., Stolowich, N., and Yappert, M. C. (2008) Influence of temperature on 31P NMR chemical shifts of phospholipids and their metabolites I. In chloroform-methanol-water. Anal. Biochem. 380, 41-50.
    • (2008) Anal. Biochem. , vol.380 , pp. 41-50
    • Estrada, R.1    Stolowich, N.2    Yappert, M.C.3
  • 35
    • 42649130559 scopus 로고
    • New compensated Carr-Purcell sequences
    • Gullion, T., Baker, D. B., and Conradi, M. S. (1990) New compensated Carr-Purcell sequences. J. Magn. Reson. 89, 479-484.
    • (1990) J. Magn. Reson. , vol.89 , pp. 479-484
    • Gullion, T.1    Baker, D.B.2    Conradi, M.S.3
  • 36
    • 85011817347 scopus 로고
    • Detection of weak heteronuclear dipole coupling by rotational-echo double-resonance nuclear magnetic resonance
    • Gullion, T., and Schaefer, J. (1989) Detection of weak heteronuclear dipole coupling by rotational-echo double-resonance nuclear magnetic resonance. Adv. Magn. Reson. 13, 57-83.
    • (1989) Adv. Magn. Reson. , vol.13 , pp. 57-83
    • Gullion, T.1    Schaefer, J.2
  • 37
    • 45149145322 scopus 로고
    • Rotational-echo doubleresonance NMR
    • Gullion, T., and Schaefer, J. (1989) Rotational-echo doubleresonance NMR. J. Magn. Reson. 81, 196-200.
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 39
    • 23244440382 scopus 로고    scopus 로고
    • 13C chemical shift anisotropies as experimental restraints
    • DOI 10.1529/biophysj.105.059857
    • Soubias, O., Jolibois, F., Massou, S., Milon, A., and Réat, V. (2005) Determination of the orientation and dynamics of ergosterol in model membranes using uniform 13C labeling and dynamically averaged 13C chemical shift anisotropies as experimental restraints. Biophys. J. 89, 1120-1131. (Pubitemid 41098994)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1120-1131
    • Soubias, O.1    Jolibois, F.2    Massou, S.3    Milon, A.4    Reat, V.5
  • 40
    • 33748560477 scopus 로고    scopus 로고
    • Modulation of amphotericin B membrane interaction by cholesterol and ergosterol - A molecular dynamics study
    • DOI 10.1021/jp061916g
    • A few recent examples are: (a) Czub, J., and Baginski, M. (2006) Modulation of amphotericin B membrane interaction by cholesterol and ergosterols-a molecular dynamics Study. J. Phys. Chem. B 110, 16743-16753. (Pubitemid 44373404)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.33 , pp. 16743-16753
    • Czub, J.1    Baginski, M.2
  • 41
    • 62549150286 scopus 로고    scopus 로고
    • Molecular modeling of amphotericin B-ergosterol primary complex in water II
    • Baran, M., Borowski, E., and Mazerski, J. (2009) Molecular modeling of amphotericin B-ergosterol primary complex in water II. Biophys. Chem. 141, 162-168.
    • (2009) Biophys. Chem. , vol.141 , pp. 162-168
    • Baran, M.1    Borowski, E.2    Mazerski, J.3
  • 42
    • 0030947228 scopus 로고    scopus 로고
    • A formal synthesis of brassinolide
    • DOI 10.1016/S0040-4039(97)00474-7, PII S0040403997004747
    • Schmittberger, T., and Uguen, D. (1997) A formal synthesis of brassinolide. Tetrahedron Lett. 38, 2837-2840. (Pubitemid 27156864)
    • (1997) Tetrahedron Letters , vol.38 , Issue.16 , pp. 2837-2840
    • Schmittberger, T.1    Uguen, D.2
  • 43
    • 0035907721 scopus 로고    scopus 로고
    • Total synthesis of agosterol A: An MDR-modulator from a marine sponge
    • DOI 10.1002/1521-3765(20010618)7:12<2663::AID-CHEM26630>3.0.CO;2-U
    • Murakami, N., Sugimoto, M., Morita, M., and Kobayashi, M. (2001) Total synthesis of agosterol A: an MDR-modulator from a marine sponge. Chem.?Eur. J. 7, 2663-2670. (Pubitemid 32587737)
    • (2001) Chemistry - A European Journal , vol.7 , Issue.12 , pp. 2663-2670
    • Murakami, N.1    Sugimoto, M.2    Morita, M.3    Kobayashi, M.4
  • 45
    • 0001956960 scopus 로고
    • Analytic solutions for the time evolution of dipolar-dephasing NMR signals
    • Mueller, K. T. (1995) Analytic solutions for the time evolution of dipolar-dephasing NMR signals. J. Magn. Reson. 113, 81-93.
    • (1995) J. Magn. Reson. , vol.113 , pp. 81-93
    • Mueller, K.T.1
  • 46
    • 33646174649 scopus 로고    scopus 로고
    • Comparative molecular dynamics study of lipid membranes containing cholesterol and ergosterol
    • Czub, J., and Baginski, M. (2006) Comparative molecular dynamics study of lipid membranes containing cholesterol and ergosterol. Biophys. J. 90, 2368-2382.
    • (2006) Biophys. J. , vol.90 , pp. 2368-2382
    • Czub, J.1    Baginski, M.2
  • 47
    • 77950658500 scopus 로고    scopus 로고
    • Active amphotericin B derivatives position the mycosamine in two radial orientations
    • Volmer, A. A., and Carreira, E. M. (2010) Active amphotericin B derivatives position the mycosamine in two radial orientations. ChemBioChem 11, 778-781.
    • (2010) ChemBioChem , vol.11 , pp. 778-781
    • Volmer, A.A.1    Carreira, E.M.2
  • 48
    • 79953728167 scopus 로고    scopus 로고
    • Channels formed by amphotericin B covalent dimers exhibit rectification
    • Hirano, M., Takeuchi, Y., Matsumori, N., Murata, M., and Ide, T. (2011) Channels formed by amphotericin B covalent dimers exhibit rectification. J. Membr. Biol. 240, 159-164.
    • (2011) J. Membr. Biol. , vol.240 , pp. 159-164
    • Hirano, M.1    Takeuchi, Y.2    Matsumori, N.3    Murata, M.4    Ide, T.5
  • 49
    • 0033568053 scopus 로고    scopus 로고
    • Centerband-only detection of exchange: Efficient analysis of dynamics in solids by NMR
    • DOI 10.1021/ja992022v
    • deAzevedo, E. R., Hu, W. G., Bonagamba, T. J., and Schmidt-Rohr, K. (1999) Centerband-only detection of exchange: Efficient analysis of dynamics in solids by NMR. J. Am. Chem. Soc. 121, 8411-8412. (Pubitemid 29444490)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.36 , pp. 8411-8412
    • DeAzevedo, E.R.1    Hu, W.-G.2    Bonagamba, T.J.3    Schmidt-Rohr, K.4
  • 50
    • 33744941313 scopus 로고    scopus 로고
    • 1H-driven spin diffusion NMR spectroscopy
    • DOI 10.1021/ja0603406
    • Luo, W., and Hong, M. (2006) Determination of the Oligomeric Number and Intermolecular Distances of Membrane Protein Assemblies by Anisotropic 1H-Driven Spin Diffusion NMR Spectroscopy. J. Am. Chem. Soc. 128, 7242-7251. (Pubitemid 43849126)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.22 , pp. 7242-7251
    • Luo, W.1    Hong, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.